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  • Fatouma Touré, Jean-Marie Zahm, +7 authors Philippe Rieu
  • Biology, Medicine
  • The Biochemical journal
  • 2008 (First Published: 1 December 2008)
  • AGEs (advanced glycation end-products) accumulate in collagen molecules during uraemia and diabetes, two diseases associated with high susceptibility to bacterial infection. Because neutrophils bindContinue Reading
  • Roselyne Garnotel, Jean Claude Monboisse, Alain Randoux, B Muller Haye, J. P. Borel
  • Biology, Medicine
  • The Journal of biological chemistry
  • 1995 (First Published: 17 November 1995)
  • Monoclonal antibodies to the alpha L beta 2 integrin inhibit the binding of type I collagen to PMN (polymorphonuclear neutrophil leukocytes) as well as the subsequent stimulation of superoxideContinue Reading
  • Stéphane Poitevin, Roselyne Garnotel, Franck Antonicelli, Philippe Gillery, P Nguyen
  • Medicine
  • Journal of thrombosis and haemostasis : JTH
  • 2008 (First Published: 1 September 2008)
  • BACKGROUND Tissue factor (TF), the main trigger of coagulation cascade, is a major component of the atherosclerotic plaque. Matrix metalloproteinases (MMPs) are recognized as key mediators ofContinue Reading
  • Stéphane Jaisson, Céline Delevallée-Forte, Fatouma Touré, Philippe Rieu, Roselyne Garnotel, Philippe Gillery
  • Chemistry, Medicine
  • FEBS letters
  • 2007 (First Published: 3 April 2007)
  • Carbamylation is a post-translational modification of proteins characterized by the binding of cyanate to amino groups, increased in renal failure. Pathophysiological consequences of carbamylationContinue Reading
  • Stéphane Jaisson, Véronique Larreta-Garde, Georges Bellon, William Hornebeck, Roselyne Garnotel, Philippe Gillery
  • Biology, Medicine
  • Matrix biology : journal of the International…
  • 2007 (First Published: 1 April 2007)
  • Carbamylation is a post-translational modification due to nonenzymatic binding of cyanate, a by-product of urea, on free amino groups of proteins. Post-translational modifications are known to induceContinue Reading